Factors Affecting Enzyme Activity: 5 Factors

(1) Concentration of Enzyme (2) Concentration of Substrate (3) Effect of

Temperature (4) Effect of pH (5) Effect of Product Concentration

The metabolic network is intricate and constructed to ensure that metabolic

responses are specific in timing and circumstances. Regulatory enzymes contribute to
the timing aspect by controlling the overall rate of a metabolic pathway. How the cell
reacts to a certain event depends on the availability of metabolites and the catalytic
activity of the enzymes within the route. In doing so, enzymatic reactions transpire
only in suitable cellular environments and proceed at a rate appropriate to the
availability of the necessary substrate or cofactors. Changes in the surrounding
conditions are reflected in certain factors, promoting or suppressing the enzyme’s
activity and the rate of enzymatic reactions.

Factor 1. Concentration of Enzyme:

By lowering the activation energy and stabilizing the transition state, the temporary
bonds between enzymes and their substrates catalyze the processes. A higher enzyme
concentration simply means that there are more enzyme molecules available to break
down the substrate. High concentrations of the enzyme-substrate complex cause a
greater initial catalytic rate, which helps the reaction move more quickly toward
reactant-product equilibrium..

As the concentration of the enzyme is increased, the velocity of the reaction

proportionately increases (Fig. 66.1). In fact, this property of enzyme is made use in
determining the activities of serum enzymes for diagnosis of diseases.

Factor 2. Concentration of Substrate:

Increase in the substrate concentration gradually increases the velocity of enzyme
reaction within the limited range of substrate levels. A rectangular hyperbola is
obtained when velocity is plotted against the substrate concentration (Fig. 66.2).
Three distinct phases of the reaction are observed in the graph.

Substrate concentration is the amount of substrate present that can be turned into
product and is most commonly measured in molarity (moles per liter). The
concentration of substrates is often used to measure enzyme activity, which is based
on the rate of a reaction (product formed over time).

Factor 3. Effect of Temperature:

Velocity of an enzyme reaction increases with increase in temperature up to a

maximum and then declines. A bell-shaped curve is usually observed (Fig. 66.4).

The optimum temperature for most of the enzymes is between 40°C-45°C. Even so,
deviations from the ideal temperature of a few degrees only slightly reduce the
activity of the enzyme. As the reactants gain more kinetic energy, a little rise in
temperature can hasten the rate of the reaction. But when the temperature is much off,
the enzyme activity is significantly diminished. The enzyme's structure and
intramolecular linkages may be destroyed by extremely high temperatures, rendering
it irreversibly inactive. However, when the temperature drops below the water's
freezing point (0°C or 32°F), ice crystals start to form, which can permanently harm
the proteins. When frozen enzymes are thawed, the same result is also observed.

Factor 4. Effect of pH:

Increase in the hydrogen ion concentration (pH) considerably influences the enzyme
activity and a bell-shaped curve is normally obtained (Fig. 66.5). Each enzyme has an
optimum pH at which the velocity is maximum.

Most of the enzymes of higher organisms show optimum activity around neutral pH
(6-8). There are, however, many exceptions like pepsin (1-2), acid phosphatase (4-5)
and alkaline phosphatase (10-11) for optimum pH. As a chain of amino acids,
proteins such as enzymes contain electrical charges from the sequence of their amino
acid residues. Most amino acids in the chain are the basis for the intramolecular
interactions that give the enzyme its three-dimensional structure.

Amino acids determine the substrate specificity and restrict the enzyme activity only
to a narrow range of pH. Most enzymes function optimally in slightly acidic or basic
pH. For this reason, a change in the pH value, either acidic or basic, affects the
ionization of amino acid residues, leading to changes in the three-dimensional
structure of the enzyme. The alteration in the enzyme conformation affects its
interaction with its substrate, thus reducing its activity.

Factor 5. Effect of Product Concentration:

The accumulation of reaction products generally decreases the enzyme velocity. For
certain’ enzymes, the products combine with the active site of enzyme and form a
loose complex and, thus, inhibit the enzyme activity. In the living system, this type of
inhibition is generally prevented by a quick removal of products formed

https://conductscience.com/factors-that-affect-enzyme-activity/
https://www.biologydiscussion.com/enzymes/factors-affecting-enzyme-activity-6-
factors/11207